ID GLMS_BRADU Reviewed; 608 AA.
AC P59362;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE EC=2.6.1.16;
DE AltName: Full=D-fructose-6-phosphate amidotransferase;
DE AltName: Full=GFAT;
DE AltName: Full=Glucosamine-6-phosphate synthase;
DE AltName: Full=Hexosephosphate aminotransferase;
DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase;
GN Name=glmS; OrderedLocusNames=bll4607;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; BA000040; BAC49872.1; -; Genomic_DNA.
DR RefSeq; NP_771247.1; NC_004463.1.
DR RefSeq; WP_011087378.1; NZ_CP011360.1.
DR AlphaFoldDB; P59362; -.
DR SMR; P59362; -.
DR STRING; 224911.AAV28_20270; -.
DR EnsemblBacteria; BAC49872; BAC49872; BAC49872.
DR GeneID; 64024360; -.
DR KEGG; bja:bll4607; -.
DR PATRIC; fig|224911.44.peg.4408; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_5; -.
DR InParanoid; P59362; -.
DR OrthoDB; 9761808at2; -.
DR PhylomeDB; P59362; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR CDD; cd00714; GFAT; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR HAMAP; MF_00164; GlmS; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR005855; GFAT.
DR InterPro; IPR047084; GFAT_N.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR NCBIfam; TIGR01135; glmS; 1.
DR PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 3: Inferred from homology;
KW Aminotransferase; Cytoplasm; Glutamine amidotransferase;
KW Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..608
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing]"
FT /id="PRO_0000135307"
FT DOMAIN 2..217
FT /note="Glutamine amidotransferase type-2"
FT DOMAIN 284..423
FT /note="SIS 1"
FT DOMAIN 456..598
FT /note="SIS 2"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 603
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 608 AA; 66370 MW; A2627F79781AF783 CRC64;
MCGIVGILGR EPVAEQLVDS LKRLEYRGYD SAGVATLEGR HLERRRAEGK LKNLEKRLEA
EPLKGTTGIG HTRWATHGKP TVNNAHPHAT ERVAVVHNGI IENFRELREE LEKNGTVFHT
ETDTEIVLHL VDDLLTRGNK PVEAVKLALA RLRGAFALGF IFAGDNDLMI GARNGPPLAI
GYGDGEMYLG SDAIALGPFT DTISYLEDGD WVVLTRNSAT IFDKDGHAVQ REKIKHAAST
SLVDKANYRH FMAKEIHEQP EVVGHTLARY VDMATERVSL PVKLPFDFKN IQRINITACG
TASYAGFVAK YWFERFARLP VEVDVASEFR YREAPLRKGD LAIFISQSGE TADTLAALRY
AKAEGVHTVA VVNVPTSTIA RESETVLPTL AGPEIGVAST KAFTCQLMVL ANLAIAAGKA
RGELSDEDET KLVHGLVEIP RLMSDALTTE LQIEKLAREI AKSRDVLYLG RGTSFPLALE
GALKLKEISY IHAEGYAAGE LKHGPIALID ETMPVVVIAP YDRVFEKTVS NMQEVAARGG
KIILMTDAKG AEEATVESLV TIVMPDMAAA FTPMVYAVPV QLLAYHTAVI MGTDVDQPRN
LAKSVTVE
//
